Evidence map›Paper›PMID 19836329›Full record

ReviewStructure (London, England : 1993)2009

Structure and signaling mechanism of Per-ARNT-Sim domains.

Andreas Möglich, Rebecca A Ayers, Keith Moffat

Open access · bronzeAbstract readReview
In one paragraph

Review in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 299 papers.

0numbers the graph read from it
0cells of the map it votes in
299citing papers in PubMed
40.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

299 citing papers in PubMed, 538 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Small Molecule Regulation of CLOCK:BMAL1 DNA Binding Activity.bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Structural Basis of a Novel Heme Binding Bacterial One-Component Switch.bioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. The virulence regulatorJournal of bacteriology · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Structural assembly of the PAS domain drives the catalytic activation of metazoan PASK.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. State-dependent motion of a genetically encoded fluorescent biosensor.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Article
  19. Review
  20. Protein design accelerates the development and application of optogenetic tools.Computational and structural biotechnology journal · 2025
    Review

239 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Andreas MöglichDepartment of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, University of Chicago, 929 East 57th Street, Chicago, IL 60637, USA.
Rebecca A Ayers
Keith Moffat
University of Chicago · US

Funding

X-RAY STUDY OF HORMONE-RECEPTOR AND PROTEIN-ANTIBODY COMPLEXESP41RR007707 · NCRR · UNIVERSITY OF CHICAGO · PI YANG, XIANGZHONG · 2002 to 2011
$17.3M
TIME-RESOLVED MACROMOLECULAR CRYSTALLOGRAPHYR01GM036452 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 1986 to 2012
$4.7M
TIME-RESOLVED MACROMOLECULAR CRYSTALLOGRAPHYR37GM036452 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 1995 to 2004
$1.9M
NCRR NIH HHS P41 RR007707NIGMS NIH HHS GM 036452NIGMS NIH HHS R01 GM036452NIGMS NIH HHS R37 GM036452
6 · The paper itself

Abstract

Per-ARNT-Sim (PAS) domains serve as versatile sensor and interaction modules in signal transduction proteins. PAS sensors detect chemical and physical stimuli and regulate the activity of functionally diverse effector domains. In contrast to this chemical, physical, and functional diversity, the structure of the core of PAS domains is broadly conserved and comprises a five-stranded antiparallel beta sheet and several alpha helices. Signals originate within the conserved core and generate structural and dynamic changes predominantly within the beta sheet, from which they propagate via amphipathic alpha-helical and coiled-coil linkers at the N or C termini of the core to the covalently attached effector domain. Effector domains are typically dimeric; their activity appears to be largely regulated by signal-dependent changes in quaternary structure and dynamics. The signaling mechanisms of PAS and other signaling domains share common features, and these commonalities can be exploited to enable structure-based design of artificial photosensors and chemosensors.

Indexed as

Protein Structure, TertiarySignal TransductionAmino Acid SequenceAnimalsBinding SitesHumansModels, MolecularMolecular Sequence DataProtein Serine-Threonine KinasesPAS domain kinasesProtein Serine-Threonine Kinases

Identifiers

PMID19836329
PMCPMC3092527
OpenAlexW2160405880

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.